Crystal structure of DsrE/DsrF-like family protein (NP_342589.1) from SULFOLOBUS SOLFATARICUS at 1.49 A resolution
Joint Center for Structural Genomics (JCSG)
Single crystal Si(111) bent monochromator (horizontal focusing)
G(MSE)AQAQTQGQEEEQ(MLY)(MLY)(MLY)ILIVVTHGPEDLDRTYAPLF(MSE)ASISAS(MSE)EYETSVFF (MSE)I(MLY)GP(MLY)LLD(MLY)(MLY)WQEEER(MLY)(MLY)GGNPFIHFFD(MSE)A(MLY)ENGV(MLY) (MSE)YV(CSX)VQSL(MLY)D(MSE)CH(MSE)(MLY)EDDVVEGIELVGGSTLIDLTLEADRTLFF
GMAQAQTQGQEEEQKKKILIVVTHGPEDLDRTYAPLFMASISASMEYETSVFFMIKGPKLLDKKWQEEERKKGGNPFIHF FDMAKENGVKMYVCVQSLKDMCHMKEDDVVEGIELVGGSTLIDLTLEADRTLFF
THE STATISTICS REPORTED IN REMARK 200 WERE COMPUTED WITH XSCALE WITH FRIEDEL PAIRS KEPT SEPARATE.
5.0000% polyethylene glycol 3000, 40.0000% polyethylene glycol 400, 0.1M MES pH 6.0, NANODROP', VAPOR DIFFUSION, SITTING DROP, temperature 277K
1. THIS CONSTRUCT WAS EXPRESSED WITH AN N-TERMINAL PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE. 2. THE PROTEIN WAS REDUCTIVELY METHYLATED PRIOR TO CRYSTALLIZATION.
1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2. ATOM RECORDS CONTAIN RESIDUAL B FACTORS ONLY. 3. A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4. THE DATA IS TWINNED. THE FINAL TWIN FRACTION WAS REFINED TO 0.228 USING THE OPERATOR "K,H,-L". 5.THE PROTEIN WAS SUBJECTED TO REDUCTIVE METHYLATION PRIOR TO CRYSTALLIZATION. THE LYSINE RESIDUES HAVE BEEN MODELED AS N-DIMETHYL-LYSINE (MLY). 6. CYSTEINE 93 IS OXIDIZED AND IS MODELED AS S-OXY CYSTEINE (CSX). 7. CHLORIDE ION (CL) IS MODELED FROM THE PROTEIN BUFFER SOLUTION.
Structural Genomics, Joint Center for Structural Genomics, JCSG, Protein Structure Initiative, PSI-2, unknown function
MAQAQTQGQEEEQKKKILIVVTHGPEDLDRTYAPLFMASISASMEYETSVFFMIKGPKLLDKKWQEEERKKGGNPFIHFF DMAKENGVKMYVCVQSLKDMCHMKEDDVVEGIELVGGSTLIDLTLEADRTLFF